Hb C-Ziquinchor beta6(A3)Glu->Val;
HEMATOLOGY Normal in the heterozygote
ELECTROPHORESIS Hb X moves slightly slower than Hb A2 at alkaline pH; the same is observed in IEF
CHROMATOGRAPHY Hb X and Hb A can be separated by DEAE-cellulose or DEAE-Sephadex chromatography
STRUCTURE STUDIES Tryptic digestion of AE-betaX chain; separation of peptides by fingerprinting or cation exchange chromatography; amino acid analysis; sequencing
DNA ANALYSES Not reported; presumed mutations GAG->GTG and CCT->CGT at codons 6 and 58
FUNCTION STUDIES Normal; gelling properties of Hb X are also the same as Hb S
STABILITY Tends to become autooxidized
OCCURRENCE Found in members of an African family living in Senegal
OTHER INFORMATION Quantity in the heterozygote 29-43%; the presence of an alpha-thal allele was not evaluated; the beta58 Pro->Arg mutation is also found in Hb Dhofar
1. Goossens, M., Garel, M.C., Auvinet, J., Basset, P., Ferreira Gomes, P., Rosa, J., and Arous, N.; FEBS Lett., 58:149, 1975.
2. Hassan, W., Basset, P., Oudart, J.L., Goossens, M., and Rosa, J.: Hemoglobin, 1:487, 1977.

This material is from the book A Syllabus of Human Hemoglobin Variants (1996) by Titus H.J. Huisman, Marianne F.H. Carver, and Georgi D. Efremov, published by The Sickle Cell Anemia Foundation in Augusta, GA, USA. Copyright © 1996 by Titus H.J. Huisman. All rights reserved. Neither this work nor any part may be reproduced or transmitted in any form or by any means, electronic or mechanical, microfilming and recording, or by any information storage and retrieval systems, without written permission.